ID I0R344_9MICO Unreviewed; 724 AA.
AC I0R344;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN ORFNames=IMCC13023_00210 {ECO:0000313|EMBL:EIC92280.1};
OS Candidatus Aquiluna sp. IMCC13023.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Luna cluster; Luna-1 subcluster; Aquiluna.
OX NCBI_TaxID=1081644 {ECO:0000313|EMBL:EIC92280.1, ECO:0000313|Proteomes:UP000054510};
RN [1] {ECO:0000313|Proteomes:UP000054510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC13023 {ECO:0000313|Proteomes:UP000054510};
RX PubMed=22689238; DOI=10.1128/JB.00586-12;
RA Kang I., Lee K., Yang S.J., Choi A., Kang D., Lee Y.K., Cho J.C.;
RT "Genome sequence of "Candidatus Aquiluna" sp. strain IMCC13023, a marine
RT member of the Actinobacteria isolated from an arctic fjord.";
RL J. Bacteriol. 194:3550-3551(2012).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIC92280.1}.
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DR EMBL; AJKR01000001; EIC92280.1; -; Genomic_DNA.
DR AlphaFoldDB; I0R344; -.
DR STRING; 1081644.IMCC13023_00210; -.
DR PATRIC; fig|1081644.3.peg.22; -.
DR eggNOG; COG0209; Bacteria.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000054510; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 1.10.1650.20; -; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR013346; NrdE_NrdA_C.
DR InterPro; IPR026459; RNR_1b_NrdE.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR013554; RNR_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR NCBIfam; TIGR02506; NrdE_NrdA; 1.
DR NCBIfam; TIGR04170; RNR_1b_NrdE; 1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 1.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR Pfam; PF08343; RNR_N; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
DR PROSITE; PS00089; RIBORED_LARGE; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410};
KW Reference proteome {ECO:0000313|Proteomes:UP000054510}.
FT DOMAIN 576..598
FT /note="Ribonucleotide reductase large subunit"
FT /evidence="ECO:0000259|PROSITE:PS00089"
SQ SEQUENCE 724 AA; 82088 MW; 8882F03728BCC55F CRC64;
MANQVIELDD NGVETGKTGI ESAMSYHELN AMINLWDKDG KMQLAKDKLA VRKYFLDHVN
QNTVFFHSLK ERLDYLVENE YYEKEILDQY RFEFIEELEK LAYSKKFRFD AFMGAYKFYT
GYALKTFDGE RYLERFEDRV VMVALALAEG KEDIAISMVE EIISGRFQPA TPTFLNCGKK
QRGEFVSCFL LRIEDNMESI SRAINSALQL SKRGGGVALN LSNVREYGAP IKKIEGQSSG
IIPVMKLLED SFSYANQLGA RQGAGAVYLN AHHPDILRFL DTKRENADEK TRIKTLSIGV
VVPDITMHLA KDNEDMYLFS PYDVEKVYGV PFGDISVTEK YQEMVDDPRI KKQKIKARTL
FERIAELQFE SGYPYIMYED TVNKANPIQG RINMSNLCSE ILQVNTPTTY NADLSYDQIG
KDISCNLGSL NIAMAMDGPD LAKTIETSIR ALTSVSDQSD IVSVRSISDG NHKSHAIGLG
QMNLHGYLAR EHIHYGSEEA LDFTNIYFYT VVFNAIQASN KIAIERGSTF GNFENSTYAS
GEYFEKYVTQ VWEPKTEKVK ELFAKSGARI PTQADWKKLK TSVMAHGIYN QNLQAVPPTG
SISYINNSTS SIHPIASRIE IRKEGKLGRV YYPAPFLSED TWDYYEDAYD LGPDKTIETY
AVATQHVDQG LSLTLFFKDT ATTRDVNRAQ INAWRKGIKT IYYIRIRQQA LLGTEVDSCV
SCML
//
